GUAC_STAA9
ID GUAC_STAA9 Reviewed; 325 AA.
AC A5ISL9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=GMP reductase {ECO:0000255|HAMAP-Rule:MF_01511};
DE EC=1.7.1.7 {ECO:0000255|HAMAP-Rule:MF_01511};
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01511};
DE Short=Guanosine monophosphate reductase {ECO:0000255|HAMAP-Rule:MF_01511};
GN Name=guaC {ECO:0000255|HAMAP-Rule:MF_01511};
GN OrderedLocusNames=SaurJH9_1398;
OS Staphylococcus aureus (strain JH9).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=359786;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JH9;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Tomasz A., Richardson P.;
RT "Complete sequence of chromosome of Staphylococcus aureus subsp. aureus
RT JH9.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP
CC to IMP. It functions in the conversion of nucleobase, nucleoside and
CC nucleotide derivatives of G to A nucleotides, and in maintaining the
CC intracellular balance of A and G nucleotides. {ECO:0000255|HAMAP-
CC Rule:MF_01511}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:17185, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58053, ChEBI:CHEBI:58115,
CC ChEBI:CHEBI:58349; EC=1.7.1.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01511};
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01511}.
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DR EMBL; CP000703; ABQ49192.1; -; Genomic_DNA.
DR RefSeq; WP_000688122.1; NC_009487.1.
DR AlphaFoldDB; A5ISL9; -.
DR SMR; A5ISL9; -.
DR KEGG; saj:SaurJH9_1398; -.
DR HOGENOM; CLU_022552_5_0_9; -.
DR OMA; AYKEYFG; -.
DR GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01511; GMP_reduct_type2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005994; GuaC_type_2.
DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF036500; GMP_red_Firmic; 1.
DR TIGRFAMs; TIGR01306; GMP_reduct_2; 1.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase.
FT CHAIN 1..325
FT /note="GMP reductase"
FT /id="PRO_1000087525"
FT ACT_SITE 174
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
FT BINDING 203..226
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
SQ SEQUENCE 325 AA; 36129 MW; F8FF7A9D55552BBC CRC64;
MKIFDYEDIQ LIPNKCIVES RSECDTTIQF GPKKFKLPVV PANMQTVMNE KLAKWFAEND
YFYIMHRFDE EARIPFIKHM QNSGLFASIS VGVKKAEFDF IEKLAQEKLI PEYITIDIAH
GHSDSVINMI KHIKNHIPDS FVIAGNVGTP EGVRELENAG ADATKVGIGP GRVCITKIKT
GFGTGGWQLA ALNICSKAAR KPLIADGGIR THGDIAKSIR FGASMVMIGS LFAAHEESPG
ETVELDGKQY KEYFGSASEF QKGEHKNVEG KKMFVEHKGS LMDTLKEMQQ DLQSSISYAG
GKDLKSLRTV DYVIVRNSIF NGDRD